1ti7: Difference between revisions

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New page: left|200px<br /><applet load="1ti7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ti7, resolution 1.70Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1ti7.jpg|left|200px]]<br /><applet load="1ti7" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ti7.jpg|left|200px]]<br /><applet load="1ti7" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ti7, resolution 1.70&Aring;" />
caption="1ti7, resolution 1.70&Aring;" />
'''CRYSTAL STRUCTURE OF NMRA, A NEGATIVE TRANSCRIPTIONAL REGULATOR, IN COMPLEX WITH NADP AT 1.7A RESOLUTION'''<br />
'''CRYSTAL STRUCTURE OF NMRA, A NEGATIVE TRANSCRIPTIONAL REGULATOR, IN COMPLEX WITH NADP AT 1.7A RESOLUTION'''<br />


==Overview==
==Overview==
NmrA, a transcription repressor involved in the regulation of nitrogen, metabolism in Aspergillus nidulans,is a member of the short-chain, dehydrogenase reductase superfamily. Isothermal titration calorimetry and, differential scanning calorimetry have been used to show NmrA binds NAD+, and NADP+ with similar affinity (average KD 65 microM) but has a greatly, reduced affinity for NADH and NADPH (average KD 6.0 mM). The structure of, NmrA in a complex with NADP+ reveals how repositioning a His-37 side chain, allows the different conformations of NAD+ and NADP+ to be accommodated., Modeling NAD(P)H into NmrA indicated that steric clashes, attenuation of, electrostatic interactions, and loss of aromatic ring stacking can explain, the differing affinities of NAD(P)+/NAD(P)H. The ability of NmrA to, discriminate between the oxidized and reduced forms of the dinucleotides, may be linked to a possible role in redox sensing. Isothermal titration, calorimetry demonstrated that NmrA and a C-terminal fragment of the GATA, transcription factor AreA interacted with a 1:1 stoichiometry and an, apparent KD of 0.26 microM. NmrA was unable to bind the nitrogen, metabolite repression signaling molecules ammonium or glutamine.
NmrA, a transcription repressor involved in the regulation of nitrogen metabolism in Aspergillus nidulans,is a member of the short-chain dehydrogenase reductase superfamily. Isothermal titration calorimetry and differential scanning calorimetry have been used to show NmrA binds NAD+ and NADP+ with similar affinity (average KD 65 microM) but has a greatly reduced affinity for NADH and NADPH (average KD 6.0 mM). The structure of NmrA in a complex with NADP+ reveals how repositioning a His-37 side chain allows the different conformations of NAD+ and NADP+ to be accommodated. Modeling NAD(P)H into NmrA indicated that steric clashes, attenuation of electrostatic interactions, and loss of aromatic ring stacking can explain the differing affinities of NAD(P)+/NAD(P)H. The ability of NmrA to discriminate between the oxidized and reduced forms of the dinucleotides may be linked to a possible role in redox sensing. Isothermal titration calorimetry demonstrated that NmrA and a C-terminal fragment of the GATA transcription factor AreA interacted with a 1:1 stoichiometry and an apparent KD of 0.26 microM. NmrA was unable to bind the nitrogen metabolite repression signaling molecules ammonium or glutamine.


==About this Structure==
==About this Structure==
1TI7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Emericella_nidulans Emericella nidulans] with K, CL, NAP and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1PDS. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TI7 OCA].  
1TI7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Emericella_nidulans Emericella nidulans] with <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=NAP:'>NAP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1PDS. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TI7 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Cooper, A.]]
[[Category: Cooper, A.]]
[[Category: Dodds, A.L.]]
[[Category: Dodds, A L.]]
[[Category: Hawkins, A.R.]]
[[Category: Hawkins, A R.]]
[[Category: Johnson, C.]]
[[Category: Johnson, C.]]
[[Category: Lamb, H.K.]]
[[Category: Lamb, H K.]]
[[Category: Leslie, K.]]
[[Category: Leslie, K.]]
[[Category: Nutley, M.]]
[[Category: Nutley, M.]]
[[Category: Stammers, D.K.]]
[[Category: Stammers, D K.]]
[[Category: Thompson, P.]]
[[Category: Thompson, P.]]
[[Category: CL]]
[[Category: CL]]
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[[Category: transcriptional regulation]]
[[Category: transcriptional regulation]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:50 2008''